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| | ==CALCIUM-FREE CALMODULIN== | | ==CALCIUM-FREE CALMODULIN== |
| - | <StructureSection load='1cfd' size='340' side='right'caption='[[1cfd]], [[NMR_Ensembles_of_Models | 1 NMR models]]' scene=''> | + | <StructureSection load='1cfd' size='340' side='right'caption='[[1cfd]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1cfd]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The August 2003 RCSB PDB [http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Calmodulin'' by Shuchismita Dutta and David S. Goodsell is [http://dx.doi.org/10.2210/rcsb_pdb/mom_2003_8 10.2210/rcsb_pdb/mom_2003_8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CFD FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1cfd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The August 2003 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Calmodulin'' by Shuchismita Dutta and David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2003_8 10.2210/rcsb_pdb/mom_2003_8]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CFD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CFD FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1cfc|1cfc]]</td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1cfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfd OCA], [http://pdbe.org/1cfd PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cfd RCSB], [http://www.ebi.ac.uk/pdbsum/1cfd PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfd ProSAT]</span></td></tr> | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1cfd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cfd OCA], [https://pdbe.org/1cfd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cfd RCSB], [https://www.ebi.ac.uk/pdbsum/1cfd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cfd ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/CALM_XENLA CALM_XENLA]] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. | + | [https://www.uniprot.org/uniprot/CALM1_XENLA CALM1_XENLA] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | [[Category: RCSB PDB Molecule of the Month]] | | [[Category: RCSB PDB Molecule of the Month]] |
| | [[Category: Xenopus laevis]] | | [[Category: Xenopus laevis]] |
| - | [[Category: Bax, A]] | + | [[Category: Bax A]] |
| - | [[Category: Grzesiek, S]] | + | [[Category: Grzesiek S]] |
| - | [[Category: Klee, C B]] | + | [[Category: Klee CB]] |
| - | [[Category: Kuboniwa, H]] | + | [[Category: Kuboniwa H]] |
| - | [[Category: Ren, H]] | + | [[Category: Ren H]] |
| - | [[Category: Tjandra, N]] | + | [[Category: Tjandra N]] |
| - | [[Category: Calcium-binding protein]]
| + | |
| Structural highlights
Function
CALM1_XENLA Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The three-dimensional structure of calmodulin in the absence of Ca2+ has been determined by three- and four-dimensional heteronuclear NMR experiments, including ROE, isotope-filtering combined with reverse labelling, and measurement of more than 700 three-bond J-couplings. In analogy with the Ca(2+)-ligated state of this protein, it consists of two small globular domains separated by a flexible linker, with no stable, direct contacts between the two domains. In the absence of Ca2+, the four helices in each of the two globular domains form a highly twisted bundle, capped by a short anti-parallel beta-sheet. This arrangement is qualitatively similar to that observed in the crystal structure of the Ca(2+)-free N-terminal domain of troponin C.
Solution structure of calcium-free calmodulin.,Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A Nat Struct Biol. 1995 Sep;2(9):768-76. PMID:7552748[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Kuboniwa H, Tjandra N, Grzesiek S, Ren H, Klee CB, Bax A. Solution structure of calcium-free calmodulin. Nat Struct Biol. 1995 Sep;2(9):768-76. PMID:7552748
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